Having determined the molecular structures of lamprey hemoglobin at 2.0 A resolution and glycera (blood worm) hemoglobin at 2.5 A resolution, it is proposed to elucidate as precisely as possible the alterations of structure which accompany the binding of ligands. The method of "difference Fourier synthesis" will be employed. Exploration of conditions for the preparation of X-ray quality crystals of leg hemoglobin from soya beans will continue. Having recently crystallized earthworm hemoglobin (mol. wt. about 2 x 10 to the 6th power) it is proposed to bring these crystals up to X-ray quality and then determine their crystal lattice parameters.